Abstract
Nitrogenase, the biological catalyst that reduces atmospheric N2 to ammonia, is present in widely diverse eubacteria and archaebacteria, but not in eukaryotes. The biological nitrogen-fixation process provides about 60% of the total production of fixed nitrogen from all natural and industrial sources (1). Since 1930 (2), molybdenum was believed to have an absolutely essential role in nitrogen fixation, even though early on vanadium was demonstrated to be almost as stimulatory as Mo to the growth of bacteria on N2 (3). Over the subsequent years, first through the development of the biochemistry and then later the genetics of nitrogen fixation, the essential nature of Mo solidified. The isolation of the larger component protein of nitrogenase, the MoFe protein (or component 1) (4), with its FeMo-cofactor (5), and the discovery of nitrogen-fixation specific (nif) genes involved in Mo-specific functions, which were often found to be linked to and co-regulated with the nitrogenase structural genes, supported the supposed absolute requirement for Mo. It is clear now, however, that Mo is not essential for biological nitrogen fixation.
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Newton, W.E. (1993). Nitrogenases: Distribution, Composition, Structure and Function. In: Palacios, R., Mora, J., Newton, W.E. (eds) New Horizons in Nitrogen Fixation. Current Plant Science and Biotechnology in Agriculture, vol 17. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-2416-6_2
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DOI: https://doi.org/10.1007/978-94-017-2416-6_2
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